Ribonuclease T1 has different dimensions in the thermally and chemically denatured states: a dynamic light scattering study

Ribonuclease T1 can be unfolded and refolded without forming noticeable amounts of aggregates allowing to characterise the dimensions of a protein in different denatured states in terms of the Stokes radius R S. Upon thermal unfolding R S increases from 1.74 nm at 20°C to 2.14 nm at 60°C. By contras...

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Bibliographic Details
Published in:FEBS letters 1997-02, Vol.403 (3), p.245-248
Main Authors: Gast, Klaus, Zirwer, Dietrich, Damaschun, Hilde, Hahn, Ulrich, Müller-Frohne, Marlies, Wirth, Matthias, Damaschun, Gregor
Format: Article
Language:English
Subjects:
circular dichroism
DLS
Dynamic light scattering
Escherichia coli - enzymology
Guanidine
guanidine hydrochloride
Guanidines
GuHCl
Hot Temperature
Light
Protein Denaturation
Protein folding
Ribonuclease T1
Ribonuclease T1 - chemistry
RNase T1
Scattering, Radiation
Stokes radius
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Summary:Ribonuclease T1 can be unfolded and refolded without forming noticeable amounts of aggregates allowing to characterise the dimensions of a protein in different denatured states in terms of the Stokes radius R S. Upon thermal unfolding R S increases from 1.74 nm at 20°C to 2.14 nm at 60°C. By contrast, R S=2.40 nm was obtained at 5.3 M guanidinium chloride (GuHCl) and 20°C. Heating from 20°C to 70°C in the presence of 5.3 M GuHCl led to a 5% decrease in R S. © 1997 Federation of European Biochemical Societies.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)00058-6